Open AccessEffect of anaerobic environment on the glutathione transferase isoenzymatic pattern in Proteus mirabilis
Author(s) -
Allocati Nerino,
Aceto Antonio,
Cellini Luigina,
Masulli Michele,
Dragani Beatrice,
Petruzzelli Raffaele,
Ilio Carmine
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10236.x
Subject(s) - glutathione , proteus mirabilis , biochemistry , transferase , glutathione s transferase , isoelectric point , biology , glutathione reductase , anaerobic exercise , isozyme , isoelectric focusing , enzyme , escherichia coli , physiology , glutathione peroxidase , gene
When Proteus mirabilis was cultured anaerobically in the presence of nitrate as terminal electron acceptor, a dramatic reduction of glutathione transferase production occurred. The analysis of the glutathione affinity purified materials in terms of substrate specificity, SDS‐PAGE pattern, IEF pattern and immunoblotting revealed that a significantly different glutathione transferase pattern also occurred: two new glutathione transferase forms with an isoelectric point at pH 4.8 and 5.0 appeared. Their N‐terminal amino acid sequence analysis as well as the ability to bind to a glutathione affinity column indicate that major differences between anaerobic and aerobic glutathione transferase forms are mainly located in the C‐terminal region of the primary structure. In contrast, no significant changes occurred in the production of glutathione transferase isoenzymes when P. mirabilis was grown anaerobically in the absence of a terminal electron acceptor. These results support the idea that bacterial glutathione transferase expression is not strictly related to the absence of oxygen stress.